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Database: UniProt
Entry: A0A1F7Z3N7_9BACT
LinkDB: A0A1F7Z3N7_9BACT
Original site: A0A1F7Z3N7_9BACT 
ID   A0A1F7Z3N7_9BACT        Unreviewed;       384 AA.
AC   A0A1F7Z3N7;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Cystathionine gamma-synthase {ECO:0000313|EMBL:OGM34286.1};
GN   ORFNames=A3D01_00760 {ECO:0000313|EMBL:OGM34286.1};
OS   Candidatus Woesebacteria bacterium RIFCSPHIGHO2_02_FULL_39_13.
OC   Bacteria; Candidatus Woesebacteria.
OX   NCBI_TaxID=1802505 {ECO:0000313|EMBL:OGM34286.1, ECO:0000313|Proteomes:UP000177169};
RN   [1] {ECO:0000313|EMBL:OGM34286.1, ECO:0000313|Proteomes:UP000177169}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|RuleBase:RU362118};
CC   -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family.
CC       {ECO:0000256|RuleBase:RU362118}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OGM34286.1}.
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DR   EMBL; MGGR01000007; OGM34286.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F7Z3N7; -.
DR   STRING; 1802505.A3D01_00760; -.
DR   Proteomes; UP000177169; Unassembled WGS sequence.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0019346; P:transsulfuration; IEA:InterPro.
DR   CDD; cd00614; CGS_like; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR000277; Cys/Met-Metab_PyrdxlP-dep_enz.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR11808:SF15; CYSTATHIONINE GAMMA-LYASE; 1.
DR   PANTHER; PTHR11808; TRANS-SULFURATION ENZYME FAMILY MEMBER; 1.
DR   Pfam; PF01053; Cys_Met_Meta_PP; 1.
DR   PIRSF; PIRSF001434; CGS; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR001434-2}.
FT   MOD_RES         201
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   384 AA;  42064 MW;  977548EE77C740E1 CRC64;
     MKYNTKIIQE GEKPNLKEGA YGDVSIPIHL SSTFARKEVE TPTGGYEYSR SGNPTRSALE
     KKLAALELAD FGLAFSSGLA ATTTLLLSLT KSGDRVLASD DLYGGTKRLF NRVFDKQYSV
     KFSYVDTSNI SGLEKAIKSD TKLIWLETPT NPLLKISDIK AIAKIAKKNN ILLVVDNTFL
     SPYFQKPLTL GADIVLHSTT KYINGHCDSV GGAIMLSESN VFEKLKFNQN AVGAILSPFD
     SFLTIRGIKT LALRMERHQE NALRVANFLS THPKVLKVYY PGLPTHPGYD IAKKQMTGFG
     GMISFEIRGG ISTAKRFLSN LKLFALAESL GGVESLIEHP AKMTHASLSK QEREAVGITD
     GLIRVSVGIE DARDLVKDLK QALK
//
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